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    Acta Crystallogr D Biol Crystallogr. 1999 Mar;55(Pt 3):699-701.

    Crystallization and preliminary X-ray analysis of a new L-aminopeptidase-D-amidase/D-esterase activated by a Gly-Ser peptide bond hydrolysis.

    Bompard-Gilles C, Villeret V, Fanuel L, Joris B, Frère JM, Van Beeumen J.

    Laboratorium voor Eiwitbiochemie en Eiwitengineering, Universiteit Gent, K. L. Ledeganckstraat, 35, B-9000 Gent, Belgium.

    Ochrobactrum anthropi possesses an L-aminopeptidase (DmpA) also able to act as a D-amidase/D-esterase. DmpA (40 kDa) is activated by auto-catalyzed protein splicing liberating an alpha-amino group presumably used as a general base in the catalytic mechanism. Two crystal forms were obtained at 294 K in 13-16% PEG 2000 mono-methylether at pH 9.0, adding either 0.2 M magnesium chloride or 1 M lithium chloride. Crystals of the first form belong to the space group C2221 and diffract to 3.0 A resolution, whereas crystals of the second form belong to the space group P21212 and diffract to 2.3 A resolution. Initial screening for heavy-atom derivatives on form II crystals, has led to a well substituted Hg derivative.

    PMID: 10089474 [PubMed - indexed for MEDLINE]

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